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The cloned rat pancreatic polypeptide receptor exhibits profound differences to the orthologous receptor.

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The cloned rat pancreatic polypeptide receptor exhibits profound differences to the orthologous receptor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Starbäck, P. Lundell, I. Schober, D. A. Larhammar, D. Statnick, M. A. Johnson, D. Gehlert, D. R.
Description	Author Affiliation: Lundell I ( Department of Medical Pharmacology, Uppsala University, Sweden.);
Abstract	Pancreatic polypeptide (PP) is produced in the islets of Langerhans and released in response to meals. It belongs to a family of peptides that also includes neuropeptide Y and peptide YY. In the present communication, we describe a rat receptor with high affinity for PP, therefore named PP1. Clones for the PP1 receptor were obtained by PCR using sequence information for the neuropeptide Y receptor Y1 from several species. The PP1 receptor has 46% overall amino acid sequence identity to the rat Y1 receptor and 56% identity in the transmembrane regions. The PP1 receptor displays a pharmacological profile that is distinct from previously described neuropeptide Y-family receptors. In competition with iodinated bovine PP, it binds rat PP with an affinity (K(i)) of 0.017 nM, while the affinities for peptide YY and neuropeptide Y are substantially lower with K(i) values of 162 and 192 nM, respectively. In stably transfected CHO cells, the PP1 receptor inhibits forskolin-stimulated cAMP synthesis. Northern blot hybridizations to a panel of mRNAs detected transcripts in testis and lung. A faint band was seen in colon and total brain. In contrast, the human receptor is expressed primarily in colon and small intestine. Whereas rat and human PP1 bind PP with the same affinity, the rat receptor has much lower affinity than its human ortholog for peptide YY and neuropeptide Y. Interestingly, the amino acid sequence identity between rat and human PP1 is only 75%. Thus, the sequence, the tissue distribution, and the binding profile of the PP1 receptor differ considerably between rat and human.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Pancreatic Polypeptide Metabolism Receptors, Gastrointestinal Hormone Genetics Amino Acid Sequence Animals CHO Cells Cell Line Cloning, Molecular Cricetinae DNA Primers In Vitro Techniques Kinetics Molecular Sequence Data Polymerase Chain Reaction Recombinant Proteins Sequence Homology, Amino Acid Species Specificity Tissue Distribution Transfection Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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